|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
19-430 |
3.37e-146 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 421.81 E-value: 3.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAqVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPaadGVLALAVAGRALA 98
Cdd:COG0303 2 ISVEEALALILAAVRPLG-TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGA---NPVTLRVVGEIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHPFDGPrIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFPAAaVARGEHCRRAGEDLARGARALAAGRVVRAAD 178
Cdd:COG0303 78 GSPPPGP-LGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKP-VAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 179 LGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTA 258
Cdd:COG0303 156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 259 AAQADAVITSGGVSVGDADFTRALLATLG-DVTFASVAMRPGRPLACGRIrasgreeRAALFFGLPGNPVAVAATFIVIV 337
Cdd:COG0303 236 LAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-------GGKPVFGLPGNPVSALVTFELFV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 338 RDALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDAsGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARV 417
Cdd:COG0303 309 RPALRKLAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGV 387
|
410
....*....|...
gi 126218433 418 DAGTTVDILPFDG 430
Cdd:COG0303 388 EAGEEVEVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
21-428 |
4.26e-141 |
|
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.
Pssm-ID: 238452 [Multi-domain] Cd Length: 394 Bit Score: 408.42 E-value: 4.26e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 21 VDEARALALRFAeRVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDgaalAAPAADGVLALAVAGRALAGH 100
Cdd:cd00887 1 VEAARELLLALA-PPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVR----AADTAGASVTLRVVGEIPAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 101 PFDGPrIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFPAAaVARGEHCRRAGEDLARGARALAAGRVVRAADLG 180
Cdd:cd00887 76 PPDGP-LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKP-VKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 181 LLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAA 260
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 261 QADAVITSGGVSVGDADFTRALLATL-GDVTFASVAMRPGRPLACGRIrasgreeRAALFFGLPGNPVAVAATFIVIVRD 339
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-------GGKPVFGLPGNPVSALVTFELFVRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 340 ALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDAsGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARVDA 419
Cdd:cd00887 307 ALRKLQGAPEPEPPRVKARLAEDLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEA 385
|
....*....
gi 126218433 420 GTTVDILPF 428
Cdd:cd00887 386 GEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
19-432 |
3.52e-134 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 398.22 E-value: 3.52e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPaadgvlALAVAGRALA 98
Cdd:PRK14491 199 LSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE------SYTLVGEVLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHPFDGPRIAQHAcVRIMTGAQMPAGCDTVIPQEKVDATADVVRFpAAAVARGEHCRRAGEDLARGARALAAGRVVRAAD 178
Cdd:PRK14491 273 GHQYDGTLQAGEA-VRIMTGAPVPAGADTVVMRELATQDGDKVSF-DGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 179 LGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTA 258
Cdd:PRK14491 351 QGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 259 AAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFIVIVR 338
Cdd:PRK14491 431 AAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDS-------PFFGLPGNPVAVMVSFLQFVE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 339 DALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDASGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARVD 418
Cdd:PRK14491 504 PALRKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVN 583
|
410
....*....|....
gi 126218433 419 AGTTVDILPFDGAI 432
Cdd:PRK14491 584 AGETVTIQPLAGLL 597
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
38-186 |
1.09e-34 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 126.14 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 38 VERVAL--RDALGRVLAEDVASPFDIPAYDNAAMDGYAFDgaalaapAADGVLALAVAGRAlAGHPfDGPRIAQHACVRI 115
Cdd:pfam03453 6 EETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVR-------AADGFGASEVNPIA-AGEP-PGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126218433 116 MTGAQMPAGCDTVIPQEKVDATADVVRFPAAAVARGEHCRRAGEDLARGARALAAGRVVRAADLGLLASLG 186
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
201-339 |
4.07e-32 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 118.96 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 201 FSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGGVSVGDADFTR 280
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 281 ALLATLGDV-----------TFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFIVIVRD 339
Cdd:TIGR00177 86 EALEELGEKeipgfgefrmlSSLPVLSRPGKPATAGVRGGT-------LIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-336 |
3.01e-29 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 111.14 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 201 FSTGDELQTPGEppreggLYDSNRATLAGMLARIGVETLDLGIV--RDDPAALEGALTTAAAQADAVITSGGVSVGDADF 278
Cdd:smart00852 3 ISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126218433 279 TRALLATLGDVT--FASVAMRPGRPLACGRI--RASGREERAALFFGLPGNPVAVAATFIVI 336
Cdd:smart00852 77 TPEALAELGGREllGHGVAMRPGGPPGPLANlsGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
19-430 |
3.37e-146 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 421.81 E-value: 3.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAqVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPaadGVLALAVAGRALA 98
Cdd:COG0303 2 ISVEEALALILAAVRPLG-TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGA---NPVTLRVVGEIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHPFDGPrIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFPAAaVARGEHCRRAGEDLARGARALAAGRVVRAAD 178
Cdd:COG0303 78 GSPPPGP-LGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKP-VAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 179 LGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTA 258
Cdd:COG0303 156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 259 AAQADAVITSGGVSVGDADFTRALLATLG-DVTFASVAMRPGRPLACGRIrasgreeRAALFFGLPGNPVAVAATFIVIV 337
Cdd:COG0303 236 LAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-------GGKPVFGLPGNPVSALVTFELFV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 338 RDALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDAsGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARV 417
Cdd:COG0303 309 RPALRKLAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGV 387
|
410
....*....|...
gi 126218433 418 DAGTTVDILPFDG 430
Cdd:COG0303 388 EAGEEVEVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
21-428 |
4.26e-141 |
|
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.
Pssm-ID: 238452 [Multi-domain] Cd Length: 394 Bit Score: 408.42 E-value: 4.26e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 21 VDEARALALRFAeRVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDgaalAAPAADGVLALAVAGRALAGH 100
Cdd:cd00887 1 VEAARELLLALA-PPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVR----AADTAGASVTLRVVGEIPAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 101 PFDGPrIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFPAAaVARGEHCRRAGEDLARGARALAAGRVVRAADLG 180
Cdd:cd00887 76 PPDGP-LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKP-VKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 181 LLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAA 260
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 261 QADAVITSGGVSVGDADFTRALLATL-GDVTFASVAMRPGRPLACGRIrasgreeRAALFFGLPGNPVAVAATFIVIVRD 339
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-------GGKPVFGLPGNPVSALVTFELFVRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 340 ALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDAsGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARVDA 419
Cdd:cd00887 307 ALRKLQGAPEPEPPRVKARLAEDLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEA 385
|
....*....
gi 126218433 420 GTTVDILPF 428
Cdd:cd00887 386 GEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
19-432 |
3.52e-134 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 398.22 E-value: 3.52e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPaadgvlALAVAGRALA 98
Cdd:PRK14491 199 LSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE------SYTLVGEVLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHPFDGPRIAQHAcVRIMTGAQMPAGCDTVIPQEKVDATADVVRFpAAAVARGEHCRRAGEDLARGARALAAGRVVRAAD 178
Cdd:PRK14491 273 GHQYDGTLQAGEA-VRIMTGAPVPAGADTVVMRELATQDGDKVSF-DGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 179 LGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTA 258
Cdd:PRK14491 351 QGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 259 AAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFIVIVR 338
Cdd:PRK14491 431 AAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDS-------PFFGLPGNPVAVMVSFLQFVE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 339 DALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDASGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARVD 418
Cdd:PRK14491 504 PALRKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVN 583
|
410
....*....|....
gi 126218433 419 AGTTVDILPFDGAI 432
Cdd:PRK14491 584 AGETVTIQPLAGLL 597
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
19-429 |
6.85e-114 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 339.76 E-value: 6.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFdgaalAAPAADGVLALAVAGRALA 98
Cdd:PRK10680 8 MSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAV-----RLADLASGQPLPVAGKAFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHPFDGPRIAQhACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFPAAaVARGEHCRRAGEDLARGARALAAGRVVRAAD 178
Cdd:PRK10680 83 GQPFHGEWPAG-TCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAE-VRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 179 LGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTA 258
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 259 AAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFIVIVR 338
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNS-------WFCGLPGNPVSAALTFYQLVQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 339 DALFAMMGAEAQPLP-RYPAVCDAPINKRAGRTEYLRGRAARDASGVWRVAPAGSQSSASLKSLSDANCFIVLAHDAARV 417
Cdd:PRK10680 314 PLLAKLSGNTASGLPpRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNV 393
|
410
....*....|..
gi 126218433 418 DAGTTVDILPFD 429
Cdd:PRK10680 394 EVGEWVEVEPFN 405
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
19-428 |
1.44e-79 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 258.22 E-value: 1.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVA-QVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPAADGVLALAVAGRAL 97
Cdd:PRK14498 10 VSLEEAREILESLLSELPlGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 98 AGHPFDGPrIAQHACVRIMTGAQMPAGCDTVIPQEKVDATAD---VVRfpaAAVARGEHCRRAGEDLARGARALAAGRVV 174
Cdd:PRK14498 90 AGEAPDVE-VEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDdtvEIY---RPVAPGENVRPAGEDIVAGELILPKGTRL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 175 RAADLGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGA 254
Cdd:PRK14498 166 TPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 255 LTTAAAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFI 334
Cdd:PRK14498 246 LRKALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGK-------PVVGLPGYPVSALTIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 335 VIVRDALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDASGvWRVAPAgSQSSASLKSLSDANCFIVLAHDA 414
Cdd:PRK14498 319 EFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDG-YVAYPL-SRGSGAITSLVRADGFIEIPANT 396
|
410
....*....|....
gi 126218433 415 ARVDAGTTVDILPF 428
Cdd:PRK14498 397 EGLEAGEEVEVELF 410
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
21-428 |
1.94e-63 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 210.16 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 21 VDEARALALRFAERVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPAadgVLALaVAGRALAGH 100
Cdd:PRK14690 25 VDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQ---VLPL-IEGRAAAGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 101 PFDGpRIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADVVRFpAAAVARGEHCRRAGEDLARGARALAAGRVVRAADLG 180
Cdd:PRK14690 101 PFSG-RVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAF-HGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 181 LLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAA 260
Cdd:PRK14690 179 LLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 261 QADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASGreeraalFFGLPGNPVAVAATFIVIVRDA 340
Cdd:PRK14690 259 EADVILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVP-------VFGLPGNPVAALVCTLVFARPA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 341 LFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGRAARDASGVWRvapagSQSSASLKSLSDANCFIVLAHDAARVDAG 420
Cdd:PRK14690 332 MSLLAGEGWSEPQGFTVPAAFEKRKKPGRREYLRARLRQGHAEVFR-----SEGSGRISGLSWAEGLVELGDGARRIAPG 406
|
....*...
gi 126218433 421 TTVDILPF 428
Cdd:PRK14690 407 DPVRFIPY 414
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
14-423 |
2.27e-50 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 180.39 E-value: 2.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 14 GHTVALSVDEARALALRFAERVAQVErVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAfdgaalaAPAADGVLALAVA 93
Cdd:PLN02699 3 GKTEMISVEEALSIVLSVAARLSPVI-VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYA-------VVASDGPGEYPVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 94 GRALAGHPFDGPRIAQHACVRIMTGAQMPAGCDTVIPQEKVDATADV------VRFPAAAvARGEHCRRAGEDLARGARA 167
Cdd:PLN02699 75 TESRAGNDGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPldgskrVRILSQA-SKGQDIRPVGCDIEKDAKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 168 LAAGRVVRAADLGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPP-REGGLYDSNRATLAGMLARIGVETLDLGIVRD 246
Cdd:PLN02699 154 LKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTlGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 247 DPAALEGALTTA-AAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRI--RASGREERAALFFGLP 323
Cdd:PLN02699 234 DEEELERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIdaKSAPSNSKKMLAFGLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 324 GNPVAVAATFIVIVRDALFAMMGAEAQPLPRYPAVCDAPINKRAGRTEYLRGR---AARDASGV--WRVAPAGSQSSASL 398
Cdd:PLN02699 314 GNPVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPVRPEFHRAIirwKLNDGSGNpgFVAESTGHQMSSRL 393
|
410 420
....*....|....*....|....*
gi 126218433 399 KSLSDANCFIVLAHDAARVDAGTTV 423
Cdd:PLN02699 394 LSMKSANALLELPATGNVLSAGTSV 418
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
19-347 |
1.14e-35 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 138.02 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 19 LSVDEARALALRFAERVAQVERVALRDALGRVLAEDVASPFDIPAYDNAAMDGYAFDGAALAAPaadgvlaLAVAGRALA 98
Cdd:PRK14497 11 YSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGE-------FKVIDKIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 99 GHpFDGPRIAQHACVRIMTGAQMPAGCDTVIpqeKVDATaDVVRFPAAAVAR----GEHCRRAGEDLARGARALAAGRVV 174
Cdd:PRK14497 84 GE-FKEIHIKECEAVEVDTGSMIPMGADAVI---KVENT-KVINGNFIKIDKkinfGQNIGWIGSDIPKGSIILRKGEVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 175 RAADLGLLASLGIAEVAVRRRVRVAFFSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGA 254
Cdd:PRK14497 159 SHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 255 LTTAAAQADAVITSGGVSVGDADFTRALLATLGDVTFASVAMRPGRPLACGRIRASGreeraalFFGLPGNPVAVAATFI 334
Cdd:PRK14497 239 IKRAISVADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKP-------VIGLPGNIVSTMVVLN 311
|
330
....*....|...
gi 126218433 335 VIVRDALFAMMGA 347
Cdd:PRK14497 312 MVILEYLKSLYPS 324
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
38-186 |
1.09e-34 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 126.14 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 38 VERVAL--RDALGRVLAEDVASPFDIPAYDNAAMDGYAFDgaalaapAADGVLALAVAGRAlAGHPfDGPRIAQHACVRI 115
Cdd:pfam03453 6 EETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVR-------AADGFGASEVNPIA-AGEP-PGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126218433 116 MTGAQMPAGCDTVIPQEKVDATADVVRFPAAAVARGEHCRRAGEDLARGARALAAGRVVRAADLGLLASLG 186
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
201-339 |
4.07e-32 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 118.96 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 201 FSTGDELQTPGEPPREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGGVSVGDADFTR 280
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 281 ALLATLGDV-----------TFASVAMRPGRPLACGRIRASgreeraaLFFGLPGNPVAVAATFIVIVRD 339
Cdd:TIGR00177 86 EALEELGEKeipgfgefrmlSSLPVLSRPGKPATAGVRGGT-------LIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-336 |
3.01e-29 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 111.14 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 201 FSTGDELQTPGEppreggLYDSNRATLAGMLARIGVETLDLGIV--RDDPAALEGALTTAAAQADAVITSGGVSVGDADF 278
Cdd:smart00852 3 ISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126218433 279 TRALLATLGDVT--FASVAMRPGRPLACGRI--RASGREERAALFFGLPGNPVAVAATFIVI 336
Cdd:smart00852 77 TPEALAELGGREllGHGVAMRPGGPPGPLANlsGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
202-343 |
8.13e-29 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 110.03 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 202 STGDELqtpgeppREGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGGVSVGDADFTRA 281
Cdd:pfam00994 4 TTGDEL-------LPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126218433 282 LLATLGDVT-------FASVAMRPGRPLACGRIRASGREERAalFFGLPGNPVAVAATFIVIVRDALFA 343
Cdd:pfam00994 77 ALAELGGRElpgfeelFRGVSLKPGKPVGTAPGAILSRAGKT--VFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
201-341 |
9.48e-20 |
|
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.
Pssm-ID: 238387 [Multi-domain] Cd Length: 133 Bit Score: 84.70 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 201 FSTGDELQTpgeppreGGLYDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGGVSVGDADFTR 280
Cdd:cd00758 5 VTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126218433 281 ALLATLGDVTFAS--VAMRPGRPLACGRIrasgreeRAALFFGLPGNPVAVAATFIVIVRDAL 341
Cdd:cd00758 78 EALAELGEREAHGkgVALAPGSRTAFGII-------GKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
356-428 |
3.27e-13 |
|
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known and forms an incomplete beta barrel.
Pssm-ID: 460924 [Multi-domain] Cd Length: 72 Bit Score: 64.55 E-value: 3.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126218433 356 PAVCDAPINKRAGRTEYLRGRAARDASGVWrVAPAGSQSSASLKSLSDANCFIVLAHDAARVDAGTTVDILPF 428
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEEDGRYY-AEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
202-303 |
2.18e-09 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 56.34 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126218433 202 STGDEL---QTPgeppregglyDSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGGvsvgdadf 278
Cdd:cd00885 6 AIGDELlsgQIV----------DTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG-------- 67
|
90 100
....*....|....*....|....*
gi 126218433 279 traLLATLGDVTFASVAMRPGRPLA 303
Cdd:cd00885 68 ---LGPTHDDLTREAVAKAFGRPLV 89
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
226-279 |
2.52e-03 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 38.56 E-value: 2.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 126218433 226 TLAGMLARIGVETLDLGIVRDDPAALEGALTTAAA--QADAVITSGGVSVGDADFT 279
Cdd:COG0521 33 ALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDdeGVDLVLTTGGTGLSPRDVT 88
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
221-270 |
7.33e-03 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 38.62 E-value: 7.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 126218433 221 DSNRATLAGMLARIGVETLDLGIVRDDPAALEGALTTAAAQADAVITSGG 270
Cdd:PRK00549 19 NTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGG 68
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
227-270 |
9.70e-03 |
|
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 36.69 E-value: 9.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 126218433 227 LAGMLARIGVETLDLGIVRDDPAALEGALTTAAA--QADAVITSGG 270
Cdd:cd00886 25 LVELLEEAGHEVVAYEIVPDDKDEIREALIEWADedGVDLILTTGG 70
|
|
| |
